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Literature summary extracted from

  • Guerin, M.E.; Kaur, D.; Somashekar, B.S.; Gibbs, S.; Gest, P.; Chatterjee, D.; Brennan, P.J.; Jackson, M.
    New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB is an essential enzyme of Mycobacterium smegmatis (2009), J. Biol. Chem., 284, 25687-25696.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.346 isopropyl-1-thio-beta-D-galactopyranoside
-
Mycolicibacterium smegmatis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.346 expression in Escherichia coli BL21 Mycolicibacterium smegmatis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.346 membrane
-
Mycolicibacterium smegmatis 16020
-

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.345 Mycolicibacterium smegmatis A0QWG6
-
-
2.4.1.345 Mycolicibacterium smegmatis ATCC 700084 A0QWG6
-
-
2.4.1.346 Mycolicibacterium smegmatis A0R043
-
-
2.4.1.346 Mycolicibacterium smegmatis ATCC 700084 A0R043
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.346
-
Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.346 GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
Mycolicibacterium smegmatis GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.346 GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
Mycolicibacterium smegmatis ATCC 700084 GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.346 GDP-Man + phosphatidyl-myo-inositol assay at pH 7.5, 37°C, reaction stopped with CHCl3/CH3OH Mycolicibacterium smegmatis ?
-
?
2.4.1.346 GDP-Man + phosphatidyl-myo-inositol assay at pH 7.5, 37°C, reaction stopped with CHCl3/CH3OH Mycolicibacterium smegmatis ATCC 700084 ?
-
?
2.4.1.346 additional information PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol Mycolicibacterium smegmatis ?
-
?
2.4.1.346 additional information PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol Mycolicibacterium smegmatis ATCC 700084 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.346 mannoslytransferase PimB'
-
Mycolicibacterium smegmatis
2.4.1.346 MSMEG_4253
-
Mycolicibacterium smegmatis
2.4.1.346 PimB
-
Mycolicibacterium smegmatis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.346 37
-
assay at Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.346 7.5
-
assay at Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
2.4.1.345 physiological function both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol as a lipid acceptor. PimA specifically catalyzes the transfer of a mannopyranosyl residue to the 2-position of the myo-inositol ring of phosphatidylinositol, whereas PimB' exclusively transfers to the 6-position. PimB' can catalyze the transfer of a mannopyranosyl residue onto the phosphatidylinositol-monomannoside (PIM1) product of PimA, while PimA is unable in vitro to transfer mannopyranosyl onto the PIM1 product of PimB' Mycolicibacterium smegmatis
2.4.1.346 physiological function both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol as a lipid acceptor. PimA specifically catalyzes the transfer of a mannopyranosyl residue to the 2-position of the myo-inositol ring of phosphatidylinositol, whereas PimB' exclusively transfers to the 6-position. PimB' can catalyze the transfer of a mannopyranosyl residue onto the phosphatidylinositol-monomannoside (PIM1) product of PimA, while PimA is unable in vitro to transfer mannopyranosyl onto the PIM1 product of PimB' Mycolicibacterium smegmatis